{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ko KT"],"funding":["Medical Research Council","Wellcome Trust"],"pagination":["5603"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9509318"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["An effective malaria vaccine remains a global health priority and vaccine immunogens which prevent transmission of the parasite will have important roles in multi-component vaccines. One of the most promising candidates for inclusion in a transmission-blocking malaria vaccine is the gamete surface protein Pfs48/45, which is essential for development of the parasite in the mosquito midgut. Indeed, antibodies which bind Pfs48/45 can prevent transmission if ingested with the parasite as part of the mosquito bloodmeal. Here we present the structure of full-length Pfs48/45, showing its three domains to form a dynamic, planar, triangular arrangement. We reveal where transmission-blocking and non-blocking antibodies bind on Pfs48/45. Finally, we demonstrate that antibodies which bind across this "],"journal":["Nature communications"],"pubmed_title":["Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies."],"pmcid":["PMC9509318"],"funding_grant_id":["MR/R001138/1","220797/Z/20/Z"],"pubmed_authors":["Mekhaiel D","Miura K","Long CA","Higgins MK","Jore MM","Biswas S","Deuker DJ","Ko KT","Lennartz F","Guloglu B","Marini A"],"additional_accession":[]},"is_claimable":false,"name":"Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies.","description":"An effective malaria vaccine remains a global health priority and vaccine immunogens which prevent transmission of the parasite will have important roles in multi-component vaccines. One of the most promising candidates for inclusion in a transmission-blocking malaria vaccine is the gamete surface protein Pfs48/45, which is essential for development of the parasite in the mosquito midgut. Indeed, antibodies which bind Pfs48/45 can prevent transmission if ingested with the parasite as part of the mosquito bloodmeal. Here we present the structure of full-length Pfs48/45, showing its three domains to form a dynamic, planar, triangular arrangement. We reveal where transmission-blocking and non-blocking antibodies bind on Pfs48/45. Finally, we demonstrate that antibodies which bind across this ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-06-01T02:26:13.353Z","creation":"2026-04-08T09:13:31.349Z"},"accession":"S-EPMC9509318","cross_references":{"pubmed":["36153317"],"doi":["10.1038/s41467-022-33379-6"]}}